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Inspired by the natural PTM, we present a new approach to inhibit amyloid aggregation by chemical PTM modification. Polyoxometalates (POMs) were used as examples of inhibitors of \u03b2\u2010amyloid peptide (A\u03b2) aggregation to illustrate the chemical PTM method. After the POMs were modified with thiazolidinethione (TZ), the resulting POMD\u2010TZ acted as a chemical PTM agent and could covalently modify A\u03b2 site\u2010selectively at Lys16. Multiple biophysical techniques and biochemical assays have been employed to show the superiority of the chemical PTM method compared to traditional A\u03b2 inhibitors. Since A\u03b2 oligomers are more cytotoxic, we further functionalized POMD\u2010TZ with an A\u03b2\u2010targeted peptide and a fluorescent probe to obtain an \u201cA\u03b2 oligomer sensitive\u201d probe. The use of PTM agents for the site\u2010directed chemical modification of proteins provides a new way to regulate amyloid aggregation.<\/jats:p>","DOI":"10.1002\/anie.202115336","type":"journal-article","created":{"date-parts":[[2022,2,8]],"date-time":"2022-02-08T23:53:32Z","timestamp":1644364412000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":51,"title":["Site\u2010Directed Chemical Modification of Amyloid by Polyoxometalates for Inhibition of Protein Misfolding and Aggregation"],"prefix":"10.1002","volume":"61","author":[{"given":"Nan","family":"Gao","sequence":"first","affiliation":[{"name":"Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization Changchun Institute of Applied Chemistry Chinese Academy of Science  Changchun, Jilin 130022 P. R. China"},{"name":"School of Applied Chemistry and Engineering University of Science and Technology of China  Hefei Anhui 230026 P. R. 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